热处理对α-乳白蛋白及其与其他乳蛋白相互作用的研究进展

摘要/Abstract

摘要： 本文综述了热处理导致的α-乳白蛋白（α-lactalbumin, α-La）的变性及其与其他乳蛋白成分之间的相互作用和影响因素。α-La的热稳定性受其分子内结合的Ca2+影响，变性后无法自聚，但可以与β-乳球蛋白（β-lactoglobulin, β-Lg）和血清白蛋白（serum albumin, SA）形成聚集体。经高温短时巴氏杀菌（high temperature short time, HTST）处理生成的α-La/β-Lg聚集体可用于生产低粘度、低浊度和高溶解性的蛋白饮料，α-La/SA聚集体具有良好的凝胶结构。α-La/β-Lg聚集体又会与酪蛋白胶束表面的κ-酪蛋白结合，生成的聚合物有利于缩短生产发酵乳的时间，改善酸乳凝胶结构。α-乳白蛋白还能与免疫球蛋白G（Immunoglobulin G, IgG）结合，采用HTST、超巴氏杀菌（Ultra-pasteurization, UP）和超高温灭菌（Ultra-high temperature, UHT）处理可降低乳品的致敏性。在实际生产中可根据需要利用上述反应，选择合适的热处理方式。

关键词: α-乳白蛋白, 热处理, 热变性, 相互作用, 应用

Abstract: In this paper, the denaturation of α-lactalbumin (α-La) induced by heat treatment, the interaction with other milk protein components and the influencing factors were reviewed. The thermal stability of α-La was affected by Ca2+ binding within its molecule. It couldn’t self-aggregate after denaturation, but could form aggregates with β-lactoglobulin (β-Lg) and serum albumin (serum albumin, SA). The aggregates of α-La/β-Lg produced by high temperature short time (HTST) treatment could be used to produce protein drinks with low viscosity, low turbidity and high solubility. The aggregates of α-La/SA had good gel structure. The α-La/β-Lg aggregation would also combine with the κ-casein on the surface of the casein micelles, and the polymer produced by α-La/β-Lg and κ-casein was beneficial to produce fermented milk, which could shorten fermentation time and improve the structure of the yogurt gel. The combination of α-La and immunoglobulin G (IgG) could reduce the allergenicity of milk, with the treatment of high temperature short time (HTST), ultra-pasteurization (UP) and ultra-high temperature (UHT). A suitable heat treatment could be selected in the actual production to improve the production efficiency.

Key words: α-Lactalbumin (α-La), Heat treatment, Thermal denaturation, Interaction, Application

中图分类号:

TS252.42

赵烜李向莹秦于思陈笛王存芳. 热处理对α-乳白蛋白及其与其他乳蛋白相互作用的研究进展[J]. 食品科学, 0, (): 0-0.

Xuan ZHAO Di Chen Cun-Fang Wang. Advances in heat treatment on α-lactalbumin and its interaction with other milk protein[J]. FOOD SCIENCE, 0, (): 0-0.

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